Mitochondrial Dynamics Is a Distinguishing Feature of Skeletal Muscle Fiber Types and Regulates Organellar Compartmentalization
Open accessAbstract
Skeletal muscle fibers differentiate into specific fiber types with distinct metabolic properties determined by their reliance on oxidative phosphorylation (OXPHOS). Using in vivo approaches, we find that OXPHOS-dependent fibers, compared to glycolytic fibers, contain elongated mitochondrial networks with higher fusion rates that are dependent on the mitofusins Mfn1 and Mfn2. Switching of a glycolytic fiber to an oxidative IIA type is associated with elongation of mitochondria, suggesting that mitochondrial fusion is linked to metabolic state. Furthermore, we reveal that mitochondrial proteins are compartmentalized to discrete domains centered around their nuclei of origin. The domain dimensions are dependent on fiber type and are regulated by the mitochondrial dynamics proteins Mfn1, Mfn2, and Mff. Our results indicate that mitochondrial dynamics is tailored to fiber type physiology and provides a rationale for the segmental defects characteristic of aged and diseased muscle fibers.
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Type I muscle fibres display a different mitochondrial topology compared with type II fibres, with mitochondria appearing more elongated and 'string-like'.
“type I muscle fibres have been shown to display a different mitochondrial topology compared with type II fibres, with mitochondria appearing more elongated and ‘string-like’ [43].”
From Human skeletal muscle mitochondrial dynamics in relation to oxidative capacity and insulin sensitivity (2021) · cites this paper as [43]
The Results and Discussion describe elongated, interconnected mitochondria in type I fibres, in contrast to the punctate mitochondria of glycolytic type IIX/IIB fibres. But type IIA fibres also have elongated mitochondria resembling those in type I fibres, so the distinction does not hold for type II fibres as a whole. The supplied passages have no page numbers. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe mitochondrial network morphology, arrangement, and connectivity adapt to each fiber type's specific functional needs (e.g., OXPHOS capacity and contractility).
“Therefore, the mitochondrial network morphology, arrangement, and connectivity adapt to each fiber type's specific functional needs (e.g., OXPHOS capacity and contractility) [31, 32].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [31]
Mitochondrial morphology and dynamics differ across muscle fiber types.
“Other studies have also highlighted that mitochondrial morphology and dynamics differ across muscle fiber types [61,66,67].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [66]
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Cre reporter strains produced by targeted insertion of EYFP and ECFP into the ROSA26 locus
Srinivas, S., Watanabe, T., Lin, C.-S., William, C. M., Tanabe, Y., Jessell, T. M., & Costantini, F. (2001) · BMC Developmental Biology · doi:10.1186/1471-213x-1-4 · Cited by 3,121 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Self-citationDuring autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735 · see citing works
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235 · see citing works
Self-citationChen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211 · see citing works
Self-citationA Developmental Switch in the Response of DRG Neurons to ETS Transcription Factor Signaling
Hippenmeyer, S., Pecho‐Vrieseling, E., Sigrist, M., Portmann, T., Laengle, C., Ladle, D. R., & Arber, S. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030159 · Cited by 1,059 · see citing works
Mitochondrial dynamics and inheritance during cell division, development and disease
Mishra, P., & Chan, D. C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3877 · Cited by 1,038 · see citing works
Self-citationCalcium Ion in Skeletal Muscle: Its Crucial Role for Muscle Function, Plasticity, and Disease
Berchtold, M. W., Brinkmeier, H., & Müntener, M. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.3.1215 · Cited by 1,007 · see citing works
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
Self-citationStructural Basis of Mitochondrial Tethering by Mitofusin Complexes
Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910 · see citing works
Self-citationThe aged niche disrupts muscle stem cell quiescence
Chakkalakal, J. V., Jones, K. M., Basson, M. A., & Brack, A. S. (2012) · Nature · doi:10.1038/nature11438 · Cited by 851 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
Self-citationLegros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676 · see citing works
Mitra, K., Wunder, C., Roysam, B., Lin, G., & Lippincott‐Schwartz, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904875106 · Cited by 625 · see citing works
Adult satellite cells and embryonic muscle progenitors have distinct genetic requirements
Lepper, C., Conway, S. J., & Fan, C. (2009) · Nature · doi:10.1038/nature08209 · Cited by 580 · see citing works
OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes
Amati-Bonneau, P., Valentino, M. L., Reynier, P., Gallardo, M. E., Bornstein, B., Boissiere, A., Campos, Y., Rivera, H., de la Aleja, J. G., Carroccia, R., et al. (2008) · Brain · doi:10.1093/brain/awm298 · Cited by 520 · see citing works
Satellite-cell pool size does matter: Defining the myogenic potency of aging skeletal muscle
Shefer, G., de Mark, D. P. V., Richardson, J. B., & Yablonka‐Reuveni, Z. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.022 · Cited by 506 · see citing works
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473 · see citing works
Self-citationFry, C. S., Lee, J. D., Mula, J., Kirby, T. J., Jackson, J. R., Liu, F., Yang, L., Mendias, C. L., Dupont-Versteegden, E. E., McCarthy, J. J., et al. (2015) · Nature Medicine · doi:10.1038/nm.3710 · Cited by 432 · see citing works
Hudson, G., Amati-Bonneau, P., Blakely, E. L., Stewart, J. D., He, L., Schaefer, A. M., Griffiths, P. G., Ahlqvist, K., Suomalainen, A., Reynier, P., et al. (2008) · Brain · doi:10.1093/brain/awm272 · Cited by 428 · see citing works
WANAGAT, J., CAO, Z., PATHARE, P., & AIKEN, J. M. (2001) · The FASEB Journal · doi:10.1096/fj.00-0320com · Cited by 378 · see citing works
Cardiac and skeletal muscle adaptations to voluntary wheel running in the mouse
Allen, D. L., Harrison, B. C., Maass, A. H., Bell, M., Byrnes, W. C., & Leinwand, L. A. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.5.1900 · Cited by 377 · see citing works
Localization of muscle gene products in nuclear domains
Pavlath, G. K., Rich, K., Webster, S. G., & Blau, H. M. (1989) · Nature · doi:10.1038/337570a0 · Cited by 326 · see citing works
A Population of Myogenic Stem Cells That Survives Skeletal Muscle Aging
Collins, C. A., Zammit, P. S., Ruiz, A. P., Morgan, J. E., & Partridge, T. A. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0372 · Cited by 320 · see citing works
Muscle stem cells contribute to myofibres in sedentary adult mice
Keefe, A. C., Lawson, J. A., Flygare, S. D., Fox, Z. D., Colasanto, M. P., Mathew, S. J., Yandell, M., & Kardon, G. (2015) · Nature Communications · doi:10.1038/ncomms8087 · Cited by 279 · cited 1× · see citing works
“During postnatal development, satellite cells (a resident stem cell population of muscular tissue) can differentiate and fuse with existing myofibers, thereby providing new nuclei and organelles to the growing fiber (Keefe et al., 2015).”
Myosin heavy chain isoforms in postnatal muscle development of mice
Agbulut, O., Noirez, P., Beaumont, F., & Butler-Browne, G. S. (2003) · Biology of the Cell · doi:10.1016/s0248-4900(03)00087-x · Cited by 261 · see citing works
Nuclear domains in muscle cells
Hall, Z. W., & Ralston, E. (1989) · Cell · doi:10.1016/0092-8674(89)90597-7 · Cited by 249 · see citing works
Shoubridge, E. A., Karpati, G., & Hastings, K. E. M. (1990) · Cell · doi:10.1016/0092-8674(90)90238-a · Cited by 245 · see citing works
The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype
Rouzier, C., Bannwarth, S., Chaussenot, A., Chevrollier, A., Verschueren, A., Bonello‐Palot, N., Fragaki, K., Caño, A., Pouget, J., Pellissier, J., et al. (2011) · Brain · doi:10.1093/brain/awr323 · Cited by 243 · see citing works
Mouse lines with photo‐activatable mitochondria to study mitochondrial dynamics
Pham, A. H., McCaffery, J. M., & Chan, D. C. (2012) · genesis · doi:10.1002/dvg.22050 · Cited by 229 · see citing works
Self-citationIsolation and Culture of Skeletal Muscle Myofibers as a Means to Analyze Satellite Cells
Keire, P. A., Shearer, A. M., Shefer, G., & Yablonka‐Reuveni, Z. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-128-8_28 · Cited by 187 · see citing works
Mitochondrial fusion is frequent in skeletal muscle and supports excitation–contraction coupling
Eisner, V., Lenaers, G., & Hajnóczky, G. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312066 · Cited by 177 · see citing works
Mattenberger, Y., James, D. I., & Martinou, J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00124-8 · Cited by 123 · see citing works
Cohen, J. A., Jeffers, B. W., Faldut, D., Marcoux, M., & Schrier, R. W. (1998) · Muscle & Nerve · doi:10.1002/(sici)1097-4598(199801)21:1 · Cited by 103 · see citing works
Smooth muscle myosin heavy chain isoforms and their role in muscle physiology
Babu, G. J., Warshaw, D. M., & Periasamy, M. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20000915)50:6 · Cited by 92 · see citing works
Kemp, R. (2004) · Nucleic Acids Research · doi:10.1093/nar/gnh090 · Cited by 85 · see citing works
Casas, M., Figueroa, R., Jorquera, G., Escobar, M., Molgó, J., & Jaimovich, E. (2010) · The Journal of General Physiology · doi:10.1085/jgp.200910397 · Cited by 65 · see citing works
Tamoxifen-Independent Recombination in the RIP-CreER Mouse
Liu, Y., Suckale, J., Masjkur, J. R., Magro, M. G., Steffen, A., Anastassiadis, K., & Solimena, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013533 · Cited by 62 · see citing works
A CreER-Based Random Induction Strategy for Modeling Translocation-Associated Sarcomas in Mice
Haldar, M., Hedberg, M. L., Hockin, M. F., & Capecchi, M. R. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4127 · Cited by 43 · see citing works
Stoller, J. Z., Degenhardt, K. R., Huang, L. F., Zhou, D. D., Lu, M. M., & Epstein, J. A. (2008) · genesis · doi:10.1002/dvg.20384 · Cited by 42 · see citing works
Psx homeobox gene is X-linked and specifically expressed in trophoblast cells of mouse placenta
Chun, J.-Y., Han, Y., & Ahn, K. (1999) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199911)216:3 · Cited by 41 · see citing works
Elson, J. L., Samuels, D. C., Johnson, M. A., Turnbull, D. M., & Chinnery, P. F. (2002) · Neuromuscular Disorders · doi:10.1016/s0960-8966(02)00047-0 · Cited by 25 · see citing works
Chakkalakal, J. V., Kuang, S., Buffelli, M., Lichtman, J. W., & Sanes, J. R. (2011) · genesis · doi:10.1002/dvg.20794 · Cited by 25 · see citing works
Niwa‐Kawakita, M., Abramowski, V., Kalamarides, M., Thomas, G. D., & Giovannini, M. (2000) · genesis · doi:10.1002/(sici)1526-968x(200002)26:2 · Cited by 22 · see citing works
Barron, M. J., Chinnery, P. F., Howel, D., Blakely, E. L., Schaefer, A. M., Taylor, R. W., & Turnbull, D. M. (2005) · Neuromuscular Disorders · doi:10.1016/j.nmd.2005.06.018 · Cited by 20 · see citing works
Redenbach, D. M., Ovalle, W. K., & Bressler, B. (1988) · Histochemistry and Cell Biology · doi:10.1007/bf00500634 · Cited by 16 · see citing works
Mourkioti, F., Slonimsky, E., Huth, M., Berno, V., & Rosenthal, N. (2008) · genesis · doi:10.1002/dvg.20419 · Cited by 11 · see citing works
String mitochondria in mouse soleus muscle
Fujioka, H., Tandler, B., Haldar, S. M., Jain, M. K., & Hoppel, C. L. (2012) · Microscopy Research and Technique · doi:10.1002/jemt.22158 · Cited by 6 · see citing works
Ogata (1997) · doi:10.1002/(sici)1097-0185(199706)248:2
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Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works
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Hood, D. A., Memme, J. M., Oliveira, A. N., & Triolo, M. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114310 · Cited by 567 · see citing works
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Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494 · see citing works
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Picard, M. A., Wallace, D. C., & Burelle, Y. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.003 · Cited by 454 · see citing works
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MacVicar, T., & Langer, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.159186 · Cited by 420 · see citing works
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Halling, J. F., & Pilegaard, H. (2020) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0005 · Cited by 418 · see citing works
Bao, H., Cao, J., Chen, M., Min, C., Chen, W., Chen, X., Chen, Y., Chen, Y., Chen, Y., Chen, Z., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2305-0 · Cited by 389 · see citing works
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Gan, Z., Fu, T., Kelly, D. P., & Vega, R. B. (2018) · Cell Research · doi:10.1038/s41422-018-0078-7 · Cited by 287 · see citing works
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Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive physiology · doi:10.1002/j.2040-4603.2020.tb00136.x · Cited by 283 · see citing works
Saben, J. L., Boudoures, A. L., Shyr, Z. A., Thompson, A. S., Drury, A. M., Zhang, W., Chi, M. M.-Y., Cusumano, A., Scheaffer, S. M., & Moley, K. H. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.065 · Cited by 266 · see citing works
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“Other studies have also highlighted that mitochondrial morphology and dynamics differ across muscle fiber types [61,66,67].”
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Bloise, F. F., Cordeiro, A., & Ortiga-Carvalho, T. M. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0611 · Cited by 238 · see citing works
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Furrer, R., Hawley, J. A., & Handschin, C. (2023) · Physiological Reviews · doi:10.1152/physrev.00017.2022 · Cited by 232 · see citing works
Drake, J. C., Wilson, R. J., Laker, R. C., Guan, Y., Spaulding, H. R., Nichenko, A. S., Shen, W., Shang, H., Dorn, M. V., Huang, K. A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025932118 · Cited by 196 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
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Vincent, A. E., White, K., Davey, T., Philips, J., Ogden, R. T., Lawless, C., Warren, C., Hall, M. G., Ng, Y. S., Falkous, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.010 · Cited by 195 · see citing works
Abdelmoez, A. M., Puig, L. S., Smith, J. A. B., Gabriel, B. M., Savikj, M., Dollet, L., Chibalin, A., Krook, A., Zierath, J. R., & Pillon, N. J. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00540.2019 · Cited by 180 · see citing works
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Eisner, V., Cupo, R. R., Gao, E., Csordás, G., Slovinsky, W. S., Paillard, M., Cheng, L., Ibetti, J., Chen, S. R. W., Chuprun, J. K., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617288114 · Cited by 161 · see citing works
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Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
Yang, X., Xue, P., Chen, H., Yuan, M., Kang, Y., Duscher, D., Machens, H., & Chen, Z. (2020) · Theranostics · doi:10.7150/thno.40857 · Cited by 147 · see citing works
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Wang, T., Xu, Y., Yuan, Y., Xu, P., Zhang, C., Li, F., Wang, L., Yin, C., Zhang, L., Cai, X., et al. (2019) · EMBO Reports · doi:10.15252/embr.201947892 · Cited by 137 · see citing works
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Lin, C.-C., Kurashige, M., Liu, Y., Terabayashi, T., Ishimoto, Y., Wang, T., Choudhary, V., Hobbs, R. P., Liu, L., Lee, P., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-20856-6 · Cited by 109 · see citing works
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Halling, J. F., Ringholm, S., Olesen, J., Prats, C., & Pilegaard, H. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.05.020 · Cited by 86 · see citing works
Houzelle, A., Jörgensen, J. A., Schaart, G., Daemen, S., van Polanen, N., Fealy, C. E., Hesselink, M. K. C., Schrauwen, P., & Hoeks, J. (2021) · Diabetologia · doi:10.1007/s00125-020-05335-w · Cited by 83 · see citing works
Alessio, E., Buson, L., Chemello, F., Peggion, C., Grespi, F., Martini, P. G. V., Massimino, M. L., Pacchioni, B., Millino, C., Romualdi, C., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz007 · Cited by 82 · see citing works
Energy metabolism design of the striated muscle cell
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PGC-1α regulates mitochondrial properties beyond biogenesis with aging and exercise training
Halling, J. F., Jessen, H., Nøhr-Meldgaard, J., Buch, B. T., Christensen, N. M., Gudiksen, A., Ringholm, S., Neufer, P. D., Prats, C., & Pilegaard, H. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00059.2019 · Cited by 82 · see citing works
Mitochondrial dynamics involves molecular and mechanical events in motility, fusion and fission
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Myonuclear content regulates cell size with similar scaling properties in mice and humans
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Metabolic Networks Influencing Skeletal Muscle Fiber Composition
Julien, I. B., Sephton, C., & Dutchak, P. A. (2018) · Front. Cell Dev. Biol. · doi:10.3389/fcell.2018.00125 · Cited by 67 · see citing works
Kong, B. C., Hudson, N. J., Seo, D., Lee, S., Khatri, B., Lassiter, K., Cook, D., Piekarski, A., Dridi, S., Anthony, N. B., et al. (2017) · BMC Genomics · doi:10.1186/s12864-016-3471-y · Cited by 72 · see citing works
Spontaneous recombinase activity of Cre–ERT2 in vivo
Kristianto, J., Johnson, M. G., Zastrow, R. K., Radcliff, A. B., & Blank, R. D. (2017) · Transgenic Research · doi:10.1007/s11248-017-0018-1 · Cited by 72 · see citing works
Crupi, A. N., Nunnelee, J. S., Taylor, D. J., Thomas, A., Vit, J., Riera, C. E., Gottlieb, R. A., & Goodridge, H. S. (2018) · Aging · doi:10.18632/aging.101643 · Cited by 72 · see citing works
Chemello, F., Grespi, F., Zulian, A., Cancellara, P., Hébert-Chatelain, É., Martini, P. G. V., Bean, C., Alessio, E., Buson, L., Bazzega, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.105 · Cited by 72 · see citing works
The misogyny of iron deficiency
Dugan, C., MacLean, B., Cabolis, K., Abeysiri, S., Khong, A., Sajic, M., & Richards, T. (2021) · Anaesthesia · doi:10.1111/anae.15432 · Cited by 73 · see citing works
Latent mitochondrial DNA deletion mutations drive muscle fiber loss at old age
Herbst, A. J., Wanagat, J., Cheema, N., Widjaja, K., McKenzie, D. I., & Aiken, J. M. (2016) · Aging Cell · doi:10.1111/acel.12520 · Cited by 66 · see citing works
Mechanobiology of muscle and myofibril morphogenesis
Luis, N. M., & Schnorrer, F. (2021) · Cells and Development · doi:10.1016/j.cdev.2021.203760 · Cited by 65 · see citing works
Drake, J. C., Laker, R. C., Wilson, R. J., Zhang, M., & Yan, Z. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1559556 · Cited by 65 · see citing works
mtDNA release promotes cGAS-STING activation and accelerated aging of postmitotic muscle cells
Li, Y., Cui, J., Liu, L., Hambright, W. S., Gan, Y., Zhang, Y., Ren, S., Yue, X., Shao, L., Cui, Y., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06863-8 · Cited by 68 · see citing works
Mitochondrial dynamics in skeletal muscle insulin resistance and type 2 diabetes
Fealy, C. E., Mulya, A., Axelrod, C. L., & Kirwan, J. P. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.011 · Cited by 63 · see citing works
Spurlock, B., Tullet, J. M. A., Hartman, J. L., & Mitra, K. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110919 · Cited by 59 · see citing works
Bell, M. B., Bush, Z., McGinnis, G. R., & Rowe, G. C. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00719.2018 · Cited by 62 · see citing works
Mitochondrial dynamics define muscle fiber type by modulating cellular metabolic pathways
Yasuda, T., Ishihara, T., Ichimura, A., & Ishihara, N. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112434 · Cited by 60 · see citing works
Ferulic acid regulates muscle fiber type formation through the Sirt1/AMPK signaling pathway
Chen, X., Guo, Y., Jia, G., Zhao, H. Y., Liu, G., & Huang, Z. (2018) · Food & Function · doi:10.1039/c8fo01902a · Cited by 60 · see citing works
Afonso, J. R., Rocha‐Rodrigues, S., Clemente, F. M., Aquino, M., Nikolaidis, P. Τ., Sarmento, H., Fílter, A., Olivares-Jabalera, J., & Ramírez‐Campillo, R. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.694604 · Cited by 57 · see citing works
Redox Signaling from Mitochondria: Signal Propagation and Its Targets
Ježek, P., Holendová, B., & Plecitá-Hlavatá, L. (2020) · Biomolecules · doi:10.3390/biom10010093 · Cited by 54 · see citing works
Exercise as a Therapeutic Intervention in Gestational Diabetes Mellitus
Δίπλα, Κ., Zafeiridis, A., Mintziori, G., Boutou, A., Goulis, D. G., & Hackney, A. C. (2021) · Endocrines · doi:10.3390/endocrines2020007 · Cited by 58 · see citing works
Jones, E., Gaytan, N., Garcia, I., Herrera, A., Ramos, M., Agarwala, D., Rana, M., Innis‐Whitehouse, W., Schuenzel, E. L., & Gilkerson, R. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2421-9 · Cited by 54 · see citing works
Li, J., Zhang, S., Li, C., Zhang, X., Shan, Y., Zhang, Z., Hai, B., & Zhang, Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-72088-6 · Cited by 57 · see citing works
Heo, J., No, M., Cho, J., Choi, Y., Cho, E., Park, D., Kim, T., Kim, C., Seo, D. Y., Han, J., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202002394r · Cited by 51 · see citing works
Adiponectin receptor agonist AdipoRon improves skeletal muscle function in aged mice
Balasubramanian, P., Schaar, A. E., Gustafson, G. E., Smith, A. B., Howell, P. R., Greenman, A., Baum, S., Colman, R. J., Lamming, D. W., Diffee, G., et al. (2022) · eLife · doi:10.7554/elife.71282 · Cited by 49 · see citing works
Mitochondrial heterogeneity and adaptations to cellular needs
Granath-Panelo, M., & Kajimura, S. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01410-1 · Cited by 49 · see citing works
Kristensen, M. D., Petersen, S. M., Møller, K. E., Lund, M. T., Hansen, M., Hansen, C. N., Courraud, J., Helge, J. W., Dela, F., & Prats, C. (2018) · Acta Physiologica · doi:10.1111/apha.13100 · Cited by 46 · see citing works
Molecular and biochemical regulation of skeletal muscle metabolism
Zumbaugh, M. D., Johnson, S., Shi, T. H., & Gerrard, D. E. (2022) · Journal of Animal Science · doi:10.1093/jas/skac035 · Cited by 53 · see citing works
Implications of mitochondrial fusion and fission in skeletal muscle mass and health
Romanello, V., & Sandri, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.011 · Cited by 44 · see citing works
Lee, H., Lim, J.-Y., & Choi, S.-J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2739721 · Cited by 43 · see citing works
The fasting‐feeding metabolic transition regulates mitochondrial dynamics
Castro‐Sepúlveda, M., Morio, B., Tuñón‐Suárez, M., Jannas-Vela, S., Díaz‐Castro, F., Rieusset, J., & Zbinden‐Foncea, H. (2021) · The FASEB Journal · doi:10.1096/fj.202100929r · Cited by 43 · see citing works
Mitochondria: At the crossroads between mechanobiology and cell metabolism
Su, É., Villard, C., & Manneville, J. (2023) · Biology of the Cell · doi:10.1111/boc.202300010 · Cited by 42 · see citing works
Kitaoka, Y., Nakazato, K., & Ogasawara, R. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00465.2016 · Cited by 43 · see citing works
Luo, N., Yue, F., Jia, Z., Chen, J., Deng, Q., Zhao, Y., & Kuang, S. (2021) · The FASEB Journal · doi:10.1096/fj.202002464r · Cited by 42 · see citing works
Effects of Ketogenic Diet on Muscle Metabolism in Health and Disease
Yakupova, E. I., Bocharnikov, A. D., & Plotnikov, E. Y. (2022) · Nutrients · doi:10.3390/nu14183842 · Cited by 44 · see citing works
The enigma of an interconnected mitochondrial reticulum: new insights into mitochondrial fusion
Mattie, S., Krols, M., & McBride, H. M. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.05.004 · Cited by 40 · see citing works
Ringholm, S., Gudiksen, A., Halling, J. F., Qoqaj, A., Rasmussen, P. M., Prats, C., Plomgaard, P., & Pilegaard, H. (2022) · The Journals of Gerontology Series A · doi:10.1093/gerona/glac164 · Cited by 42 · see citing works
Klawitter, F., Ehler, J., Bajorat, R., & Patejdl, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065516 · Cited by 40 · see citing works
Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein
Lizama, B. N., Palubinsky, A. M., Raveendran, V. A., Moore, A. M., Federspiel, J. D., Codreanu, S. G., Liebler, D. C., & McLaughlin, B. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0699-18.2018 · Cited by 37 · see citing works
Qi, Z., Xia, J., Xue, X., He, Q., Ji, L., & Ding, S. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.07.005 · Cited by 37 · see citing works
Yu, T., Deuster, P. A., & Chen, Y. (2016) · The Journal of Physiology · doi:10.1113/jp272885 · Cited by 37 · see citing works
Mohiuddin, M., Lee, N. H., Moon, J. Y., Han, W. M., Anderson, S. E., Choi, J. J., Shin, E.-J., Nakhai, S. A., Trần, T. H., Aliya, B., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45923-4 · Cited by 36 · see citing works
Sahinyan, K., Blackburn, D. M., Simon, M.-M., Lazure, F., Kwan, T., Bourque, G., & Soleimani, V. D. (2022) · eLife · doi:10.7554/elife.72792 · Cited by 32 · see citing works
Exercise: a molecular tool to boost muscle growth and mitochondrial performance in heart failure?
Nijholt, K. T., Sánchez-Aguilera, P., Voorrips, S. N., de Boer, R. A., & Westenbrink, B. D. (2021) · European Journal of Heart Failure · doi:10.1002/ejhf.2407 · Cited by 36 · see citing works
Protein composition of the muscle mitochondrial reticulum during postnatal development
Kim, Y., Yang, D. S., Katti, P., & Glancy, B. C. (2019) · The Journal of Physiology · doi:10.1113/jp277579 · Cited by 35 · see citing works
Zhou, X., Li, R., Liu, X., Wang, L., Peng, H., Chan, L., Saha, P., & Hu, Z. (2016) · Scientific Reports · doi:10.1038/srep29669 · Cited by 35 · see citing works
Mitochondrial morphology and function varies across diaphragm muscle fiber types
Brown, A. D., Fogarty, M. J., & Sieck, G. C. (2021) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2021.103780 · Cited by 35 · see citing works
Castro‐Sepúlveda, M., Fernández‐Verdejo, R., Zbinden‐Foncea, H., & Rieusset, J. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155578 · Cited by 35 · see citing works
Kallabis, S., Abraham, L., Müller, S., Dzialas, V., Türk, C., Wiederstein, J. L., Bock, T., Nolte, H., Nogara, L., Blaauw, B., et al. (2020) · Skeletal Muscle · doi:10.1186/s13395-020-00226-5 · Cited by 34 · see citing works
Advances in exercise to alleviate sarcopenia in older adults by improving mitochondrial dysfunction
Zhu, Y., Zhou, X., Zhu, A., Xiong, S., Xie, J., & Bai, Z. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1196426 · Cited by 33 · see citing works
Arginine Regulates Skeletal Muscle Fiber Type Formation via mTOR Signaling Pathway
Zhou, M., Wei, Y., Feng, Y., Zhang, S., Ma, N., Wang, K., Tan, P., Zhao, Y., Zhao, J., & Ma, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116184 · Cited by 33 · see citing works
Hou, D., Zheng, X., Cai, D., You, R., Liu, J., Wang, X., Liao, X., Tan, M., Lin, L., Wang, J., et al. (2023) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-23-0382 · Cited by 32 · see citing works
Li, J., Zhang, Z., Hai, B., & Zhang, Y. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.01.036 · Cited by 33 · see citing works
The regulation of skeletal muscle fiber-type composition by betaine is associated with NFATc1/MyoD
Du, J., Shen, L., Zhang, P., Tan, Z., Xiao, C., Luo, J., Zhao, X., Yang, Q., Gu, H., Jiang, A., et al. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-018-1657-2 · Cited by 31 · see citing works
Skeletal muscle excitation-metabolism coupling
Díaz‐Vegas, A., Eisner, V., & Jaimovich, E. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.037 · Cited by 31 · see citing works
Wang, X., Wei, Z., Gu, M., Zhu, L., Hai, C., Di, A., Wu, D., Bai, C., Su, G., Liu, X., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415707 · Cited by 29 · see citing works
Key considerations for investigating and interpreting autophagy in skeletal muscle
Rahman, F. A., Baechler, B. L., & Quadrilatero, J. (2024) · Autophagy · doi:10.1080/15548627.2024.2373676 · Cited by 29 · see citing works
Zmynd17 controls muscle mitochondrial quality and whole‐body metabolism
Fujita, R., Yoshioka, K., Seko, D., Suematsu, T., Mitsuhashi, S., Senoo, N., Miura, S., Nishino, I., & Ono, Y. (2018) · The FASEB Journal · doi:10.1096/fj.201701264r · Cited by 31 · see citing works
Li, C., Zhu, Y., Liu, W., Hayashi, T., Xiang, W., He, S., Mizuno, K., Hattori, S., Fujisaki, H., & Ikejima, T. (2023) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2023.109558 · Cited by 28 · see citing works
Castro‐Sepúlveda, M., Jannas-Vela, S., Fernández‐Verdejo, R., Ávalos-Allele, D., Tapia‐Curimil, G., Villagrán, C., Quezada, N., & Zbinden‐Foncea, H. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00025.2020 · Cited by 28 · see citing works
Wang, Y., Chen, X., Huang, Z., Chen, D., Yu, B., Chen, H., Yu, J., Luo, Y., Zheng, P., & He, J. (2021) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.11157 · Cited by 28 · see citing works
- Authors
- Mishra, P., Varuzhanyan, G., Pham, A. H., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Chan, David C.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-12
- Volume
- 22
- Issue
- 6
- Pages
- 1033-1044
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4670593
- OpenAlex
- W1940751968
- Cited by
- 290
- References
- 49
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 45 · 2023: 44 · 2022: 28 · 2021: 29 · 2020: 36 · 2019: 20 · 2018: 22 · 2017: 11 · 2016: 15
- FWCI
- 6.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM062967, R25GM076162, GM062967, T32 GM0076162, R01GM110039)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- mitochondrial dynamics, skeletal muscle fiber types, mitochondrial fusion, mitofusins, Mfn1, mitofusin 2, mitochondrial fission, Mff, oxidative phosphorylation, glycolytic fibers, mitochondrial compartmentalization, muscle aging, myopathy
- MeSH terms
- Animals, Luminescent Proteins, Membrane Proteins, Mice, Transgenic, Microscopy, Electron, Mitochondria, Oxidative Phosphorylation, Muscle Fibers, Skeletal, GTP Phosphohydrolases, Mitochondrial Proteins, Mice, Gene Knock-In Techniques, Time-Lapse Imaging, Mitochondrial Dynamics
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